Spikes Für Walkingstöcke

Description: A competitive ELISA for quantitative measurement of Human Anti centriole and centrosome antibody IgG in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A quantitative ELISA kit for measuring Human in samples from biological fluids.

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Recombinant SARS-CoV-2 Spike protein S1 subunit, encompassing amino acids 16-685. This protein corresponds to SARS-CoV-2 Variant B.1.618 originally identified in India, and contains deletions Y145 and H146 as well as mutations E484K and D614G. It was constructed with a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was affinity purified.

Description: Recombinant SARS-CoV-2 Spike protein S1 subunit, encompassing amino acids 16-685. This protein corresponds to SARS-CoV2 variant B.1.429, also known as variant Epsilon originally discovered in California (USA), and contains mutations W152C, L452R and D614G. The construct also contains a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was enzymatically biotinylated using the Avi-Tag™ and affinity purified. 

Description: Recombinant SARS-CoV-2 Spike protein S1 subunit, encompassing amino acids 16-685. This protein corresponds to SARS-CoV2 variant B.1.617.2, also known as variant Delta originally discovered in India, and contains mutations T19R, G142D, R158G, L452R, T478K, D614G and P681R as well as deletion E156-F157. The construct also contains a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was affinity purified. 

Description: Recombinant SARS-CoV-2 Spike protein S1 subunit, encompassing amino acids 16-685. This protein corresponds to SARS-CoV2 variant B.1.617.2, also known as variant Delta originally discovered in India, and contains mutations T19R, G142D, R158G, L452R, T478K, D614G and P681R as well as deletion E156-F157. The construct also contains a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was affinity purified. 

Description: The Spike S1 (B.1.617 Variant) (SARS-CoV-2): ACE2 TR-FRET Assay is designed to measure the inhibition of the binding between Spike S1 (B.1.617) (SARS-CoV-2) and human ACE2 in a homogeneous 384 reaction format. This TR-FRET-based assay requires no time-consuming washing steps, making it especially suitable for high throughput screening applications. The assay procedure is straightforward and simple; the test inhibitor compound is incubated with biotinylated Spike S1, Eu-labeled ACE2, and the dye-labeled acceptor for one hour. Then the TR-FRET signal is measured using a fluorescence reader capable of measuring Time Resolved-Fluorescence Resonance Energy Transfer (TR-FRET).

Description: The Spike S1 (B.1.618 Variant) (SARS-CoV-2): ACE2 TR-FRET Assay is designed to measure the inhibition of the binding between Spike S1 (B.1.618) (SARS-CoV-2) and human ACE2 in a homogeneous 384 reaction format. This TR-FRET-based assay requires no time-consuming washing steps, making it especially suitable for high throughput screening applications. The assay procedure is straightforward and simple; the test inhibitor compound is incubated with biotinylated Spike S1, Eu-labeled ACE2, and the dye-labeled acceptor for one hour. Then the TR-FRET signal is measured using a fluorescence reader capable of measuring Time Resolved-Fluorescence Resonance Energy Transfer (TR-FRET).

Description: SARS-CoV-2 delta variant, a variant of concern (VOC), known as B.1.617.2, was detected in India in October of 2020. However, it rapidly spread all over of the world and now it is the dominant variant in the world, which account for more than 99% of the cases. This variant carries at least 13 mutations in spike protein across the sub lineages, including L452R, D614G, P681R and K417N, which can increase the affinity to the human ACE2 receptor. Enhanced transmission of the Delta variant was observed globally, which is at least 2.5 times more contagious as the other variants. The Delta variant affects the effectiveness of COVID19 vaccine and is resistant to neutralization to some extent.

Description: SARS-CoV-2 delta variant, a variant of concern (VOC), known as B.1.617.2, was detected in India in October of 2020. However, it rapidly spread all over of the world and now it is the dominant variant in the world, which account for more than 99% of the cases. This variant carries at least 13 mutations in spike protein across the sub lineages, including L452R, D614G, P681R and K417N, which can increase the affinity to the human ACE2 receptor. Enhanced transmission of the Delta variant was observed globally, which is at least 2.5 times more contagious as the other variants. The Delta variant affects the effectiveness of COVID19 vaccine and is resistant to neutralization to some extent.

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: In September of 2020 a new lineage of SARS-CoV-2, known as B.1.1.7 and named as Alpha variant, was discovered in the United Kingdom. This lineage developed 14 lineage-specific amino acid replacements and 3 deletions. These changes caused an increase in transmission of Alpha variant (B.1.1.7 lineage) by at least 50%, leading to increased disease severity and higher death rates. The effectiveness of COVID19 vaccines are not affected by the Alpha variant. One of the mutations associated with this lineage is a N501Y in the spike protein of the virus. It is believed that this mutation is able to increase the spike protein's affinity for the host ACE2 receptor and it has been associated with increased infectivity and virulence. B.1.1.7 viruses have also been shown to have a P681H mutation in the cleavage site of spike protein. This location is one of the residues that make up the furin proteolytic cleavage site between S1 and S2 in spike protein.

Description: In September of 2020 a new lineage of SARS-CoV-2, known as B.1.1.7 and named as Alpha variant, was discovered in the United Kingdom. This lineage developed 14 lineage-specific amino acid replacements and 3 deletions. These changes caused an increase in transmission of Alpha variant (B.1.1.7 lineage) by at least 50%, leading to increased disease severity and higher death rates. The effectiveness of COVID19 vaccines are not affected by the Alpha variant. One of the mutations associated with this lineage is a N501Y in the spike protein of the virus. It is believed that this mutation is able to increase the spike protein's affinity for the host ACE2 receptor and it has been associated with increased infectivity and virulence. B.1.1.7 viruses have also been shown to have a P681H mutation in the cleavage site of spike protein. This location is one of the residues that make up the furin proteolytic cleavage site between S1 and S2 in spike protein.